INF2

INF2
Identifiers
Aliases	INF2, C14orf151, C14orf173, CMTDIE, FSGS5, pp9484, inverted formin, FH2 and WH2 domain containing, inverted formin 2
External IDs	OMIM: 610982; MGI: 1917685; HomoloGene: 82406; GeneCards: INF2; OMA:INF2 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	104,722,535 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	112,615,557 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; C1 segment; ; mucosa of transverse colon; ; right coronary artery; ; gastric mucosa; ; left coronary artery; ; popliteal artery; ; tibial arteries; ; putamen; ; right frontal lobe;
	Top expressed in
	gastrula; ; superior frontal gyrus; ; olfactory tubercle; ; decidua; ; nucleus accumbens; ; stroma of bone marrow; ; primary visual cortex; ; epithelium of lens; ; transitional epithelium of urinary bladder; ; renal corpuscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	actin binding;
Cellular component	cytoplasm; perinuclear region of cytoplasm;
Biological process	regulation of mitochondrial fission; actin cytoskeleton organization; cellular component organization;
	Sources:Amigo / QuickGO
Orthologs
	64423
	70435
	ENSG00000203485
	ENSMUSG00000037679
	Q27J81
	Q0GNC1
	NM_001031714; NM_022489; NM_032714
	NM_198411
	NP_001026884; NP_071934; NP_116103
	NP_940803; NP_001361128
	Wikidata
View/Edit Human	View/Edit Mouse

Inverted formin-2 is a protein that in humans is encoded by the INF2 gene.^[5]^[6] It belongs to the protein family called the formins. It has two splice isoforms, CAAX which localizes to the endoplasmic reticulum and non-CAAX which localizes to focal adhesions and the cytoplasm with enrichment at the Golgi.^[7]^[8] INF2 plays a role in mitochondrial fission and dorsal stress fiber formation.^[9] INF2 accelerates actin nucleation and elongation by interacting with barbed ends (fast-growing ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments.^[10]

Clinical significance

It can be associated with Focal segmental glomerulosclerosis^[11] and Charcot-Marie Tooth Disease.^[12]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000203485 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000037679 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Chhabra ES, Higgs HN (September 2006). "INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization". The Journal of Biological Chemistry. 281 (36): 26754–67. doi:10.1074/jbc.M604666200. PMID 16818491.
^ "Entrez Gene: C14orf173 chromosome 14 open reading frame 173".
^ Ramabhadran V, Korobova F, Rahme GJ, Higgs HN (December 2011). "Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture". Molecular Biology of the Cell. 22 (24): 4822–33. doi:10.1091/mbc.E11-05-0457. PMC 3237625. PMID 21998196.
^ Chhabra ES, Ramabhadran V, Gerber SA, Higgs HN (May 2009). "INF2 is an endoplasmic reticulum-associated formin protein". Journal of Cell Science. 122 (Pt 9): 1430–40. doi:10.1242/jcs.040691. PMC 2721004. PMID 19366733.
^ Korobova F, Ramabhadran V, Higgs HN (January 2013). "An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2". Science. 339 (6118): 464–7. Bibcode:2013Sci...339..464K. doi:10.1126/science.1228360. PMC 3843506. PMID 23349293.
^ Gurel PS, Ge P, Grintsevich EE, Shu R, Blanchoin L, Zhou ZH, Reisler E, Higgs HN (January 2014). "INF2-mediated severing through actin filament encirclement and disruption". Current Biology. 24 (2): 156–64. Bibcode:2014CBio...24..156G. doi:10.1016/j.cub.2013.12.018. PMC 3992431. PMID 24412206.
^ Brown EJ, Schlöndorff JS, Becker DJ, Tsukaguchi H, Tonna SJ, Uscinski AL, Higgs HN, Henderson JM, Pollak MR (January 2010). "Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis". Nature Genetics. 42 (1): 72–6. doi:10.1038/ng.505. PMC 2980844. PMID 20023659.
^ Boyer O, Nevo F, Plaisier E, Funalot B, Gribouval O, Benoit G, Huynh Cong E, Arrondel C, Tête MJ, Montjean R, Richard L, Karras A, Pouteil-Noble C, Balafrej L, Bonnardeaux A, Canaud G, Charasse C, Dantal J, Deschenes G, Deteix P, Dubourg O, Petiot P, Pouthier D, Leguern E, Guiochon-Mantel A, Broutin I, Gubler MC, Saunier S, Ronco P, Vallat JM, Alonso MA, Antignac C, Mollet G (December 2011). "INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy". The New England Journal of Medicine. 365 (25): 2377–88. doi:10.1056/NEJMoa1109122. hdl:10261/57029. PMID 22187985. S2CID 17208136.

Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Bindschadler M, McGrath JL (October 2004). "Formin' new ideas about actin filament generation". Proceedings of the National Academy of Sciences of the United States of America. 101 (41): 14685–6. Bibcode:2004PNAS..10114685B. doi:10.1073/pnas.0406317101. PMC 522045. PMID 15466701.
Fu GK, Wang JT, Yang J, Au-Young J, Stuve LL (July 2004). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000203485 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000037679 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid16818491-5] Chhabra ES, Higgs HN (September 2006). "INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization". The Journal of Biological Chemistry. 281 (36): 26754–67. doi:10.1074/jbc.M604666200. PMID 16818491.

[entrez-6] "Entrez Gene: C14orf173 chromosome 14 open reading frame 173".

[7] Ramabhadran V, Korobova F, Rahme GJ, Higgs HN (December 2011). "Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture". Molecular Biology of the Cell. 22 (24): 4822–33. doi:10.1091/mbc.E11-05-0457. PMC 3237625. PMID 21998196.

[8] Chhabra ES, Ramabhadran V, Gerber SA, Higgs HN (May 2009). "INF2 is an endoplasmic reticulum-associated formin protein". Journal of Cell Science. 122 (Pt 9): 1430–40. doi:10.1242/jcs.040691. PMC 2721004. PMID 19366733.

[9] Korobova F, Ramabhadran V, Higgs HN (January 2013). "An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2". Science. 339 (6118): 464–7. Bibcode:2013Sci...339..464K. doi:10.1126/science.1228360. PMC 3843506. PMID 23349293.

[10] Gurel PS, Ge P, Grintsevich EE, Shu R, Blanchoin L, Zhou ZH, Reisler E, Higgs HN (January 2014). "INF2-mediated severing through actin filament encirclement and disruption". Current Biology. 24 (2): 156–64. Bibcode:2014CBio...24..156G. doi:10.1016/j.cub.2013.12.018. PMC 3992431. PMID 24412206.

[11] Brown EJ, Schlöndorff JS, Becker DJ, Tsukaguchi H, Tonna SJ, Uscinski AL, Higgs HN, Henderson JM, Pollak MR (January 2010). "Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis". Nature Genetics. 42 (1): 72–6. doi:10.1038/ng.505. PMC 2980844. PMID 20023659.

[12] Boyer O, Nevo F, Plaisier E, Funalot B, Gribouval O, Benoit G, Huynh Cong E, Arrondel C, Tête MJ, Montjean R, Richard L, Karras A, Pouteil-Noble C, Balafrej L, Bonnardeaux A, Canaud G, Charasse C, Dantal J, Deschenes G, Deteix P, Dubourg O, Petiot P, Pouthier D, Leguern E, Guiochon-Mantel A, Broutin I, Gubler MC, Saunier S, Ronco P, Vallat JM, Alonso MA, Antignac C, Mollet G (December 2011). "INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy". The New England Journal of Medicine. 365 (25): 2377–88. doi:10.1056/NEJMoa1109122. hdl:10261/57029. PMID 22187985. S2CID 17208136.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

Clinical significance

References

Further reading